Interaction mechanisms of MXene with bacterial division proteins: towards efficient antibacterial materials

The rising threat of bacterial infections, coupled with the rise of antibiotic-resistant strains, has driven the search for alternative antibacterial strategies that do not rely on traditional chemical agents. Among these, antibacterial materials, particularly those based on two-dimensional nanomaterials, have emerged as promising platforms for preventing bacterial adhesion and proliferation. In this context, MXenes, a class of transition metal carbides and nitrides, have recently gained attention for their potent antibacterial properties. However, the molecular-level mechanisms by which MXenes interact with key bacterial components remain poorly understood. This study employs classical molecular dynamics (MD) simulations to investigate the interactions of Ti₃C₂O₂ MXene with bacterial membrane proteins such as FtsP and EnvC, which are involved in bacterial cell division. Results indicate that both examined proteins adsorb onto the MXene surface. Specific amino acids close to the Ti₃C₂O₂ MXene surface are identified as the main interaction sites that are the driving force for the adsorption of the proteins. Our findings demonstrate that Ti₃C₂O₂ MXene effectively interacts with bacterial membrane proteins, with FtsP exhibiting stronger adsorption than EnvC. These protein-surface interactions could be relevant to the antibacterial activity of Ti₃C₂O₂ MXene and may contribute to its potential effects on bacterial cell division.

MD simulations were performed using GROMACS 2022.2 with the CHARMM27 force field for proteins (FtsP: 2UXT, EnvC: 4BH5) and literature-derived parameters for Ti₃C₂O₂. Systems were solvated in TIP3P water, neutralized, and simulated for 200 ns at 310 K. Adsorption was analyzed through contact area and interaction energies (LJ/Coulomb), while protein stability/flexibility was assessed via RMSD, RMSF, and Rg using VMD and GROMACS tools.